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PMID: 8089174 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Microsomal aldehyde dehydrogenase is localized to the endoplasmic reticulum via its carboxyl-terminal 35 amino acids.

The Journal of cell biology ·Vol. 126 ·No. 6 ·1994-09-00 ·Pages 1407-20

Masaki R, Yamamoto A, Tashiro Y

Abstract

Rat microsomal aldehyde dehydrogenase (msALDH) has no amino-terminal signal sequence, but instead it has a characteristic hydrophobic domain at the carboxyl terminus (Miyauchi, K., R. Masaki, S. Taketani, A. Yamamoto, A. Akayama, and Y. Tashiro. 1991. J. Biol. Chem. 266:19536-19542). This membrane-bound enzyme is a useful model protein for studying posttranslational localization to its final destination. When expressed from cDNA in COS-1 cells, wild-type msALDH is localized exclusively in the well-developed ER. The removal of the hydrophobic domain results in the cytosolic localization of truncated proteins, thus suggesting that the portion is responsible for membrane anchoring. The last 35 amino acids of msALDH, including the hydrophobic domain, are sufficient for targeting of E. coli beta-galactosidase to the ER membrane. Further studies using chloramphenicol acetyltransferase fusion proteins suggest that two hydrophilic sequences on either side of the hydrophobic domain play an important role in ER targeting.

MeSH Terms
Aldehyde Dehydrogenase/chemistry,metabolism Amino Acid Sequence Animals Base Sequence Biological Transport/physiology Cell Line Endoplasmic Reticulum/enzymology,ultrastructure Microsomes/enzymology Molecular Sequence Data Mutagenesis Protein Sorting Signals/physiology Rats Recombinant Fusion Proteins/metabolism
Chemicals
Protein Sorting Signals Recombinant Fusion Proteins Aldehyde Dehydrogenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Masaki R
Department of Physiology, Kansai Medical University, Osaka, Japan.
Yamamoto A
Tashiro Y
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.126.6.1407
Published
1994-09-00
Pages
1407-20
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2290952
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.126.6.1407 PMC Full Text View journal details
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